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Database: UniProt
Entry: F1A1M6_DICPU
LinkDB: F1A1M6_DICPU
Original site: F1A1M6_DICPU 
ID   F1A1M6_DICPU            Unreviewed;       440 AA.
AC   F1A1M6;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2011, sequence version 1.
DT   27-MAR-2024, entry version 57.
DE   RecName: Full=alpha-L-fucosidase {ECO:0000256|ARBA:ARBA00012662};
DE            EC=3.2.1.51 {ECO:0000256|ARBA:ARBA00012662};
GN   ORFNames=DICPUDRAFT_58554 {ECO:0000313|EMBL:EGC29909.1};
OS   Dictyostelium purpureum (Slime mold).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=5786 {ECO:0000313|EMBL:EGC29909.1, ECO:0000313|Proteomes:UP000001064};
RN   [1] {ECO:0000313|Proteomes:UP000001064}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=QSDP1 {ECO:0000313|Proteomes:UP000001064};
RX   PubMed=21356102; DOI=10.1186/gb-2011-12-2-r20;
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Sucgang R., Kuo A., Tian X., Salerno W., Parikh A., Feasley C.L., Dalin E.,
RA   Tu H., Huang E., Barry K., Lindquist E., Shapiro H., Bruce D., Schmutz J.,
RA   Salamov A., Fey P., Gaudet P., Anjard C., Babu M.M., Basu S.,
RA   Bushmanova Y., van der Wel H., Katoh-Kurasawa M., Dinh C., Coutinho P.M.,
RA   Saito T., Elias M., Schaap P., Kay R.R., Henrissat B., Eichinger L.,
RA   Rivero F., Putnam N.H., West C.M., Loomis W.F., Chisholm R.L., Shaulsky G.,
RA   Strassmann J.E., Queller D.C., Kuspa A., Grigoriev I.V.;
RT   "Comparative genomics of the social amoebae Dictyostelium discoideum and
RT   Dictyostelium purpureum.";
RL   Genome Biol. 12:R20.1-R20.23(2011).
CC   -!- FUNCTION: Alpha-L-fucosidase is responsible for hydrolyzing the alpha-
CC       1,6-linked fucose joined to the reducing-end N-acetylglucosamine of the
CC       carbohydrate moieties of glycoproteins.
CC       {ECO:0000256|ARBA:ARBA00004071}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a neolactoside IV(2)-alpha-Fuc-nLc4Cer(d18:0) + H2O = a
CC         neolactoside nLc4Cer(d18:0) + L-fucose; Xref=Rhea:RHEA:49308,
CC         ChEBI:CHEBI:2181, ChEBI:CHEBI:15377, ChEBI:CHEBI:91119,
CC         ChEBI:CHEBI:91121; Evidence={ECO:0000256|ARBA:ARBA00000419};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49309;
CC         Evidence={ECO:0000256|ARBA:ARBA00000419};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a neolactoside IV(2)-alpha-Fuc-nLc4Cer(d18:1(4E)) + H2O = a
CC         neolactoside nLc4Cer(d18:1(4E)) + L-fucose; Xref=Rhea:RHEA:48224,
CC         ChEBI:CHEBI:2181, ChEBI:CHEBI:15377, ChEBI:CHEBI:17006,
CC         ChEBI:CHEBI:28691; Evidence={ECO:0000256|ARBA:ARBA00000321};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48225;
CC         Evidence={ECO:0000256|ARBA:ARBA00000321};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 29 family.
CC       {ECO:0000256|ARBA:ARBA00007951, ECO:0000256|PIRNR:PIRNR001092}.
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DR   EMBL; GL871378; EGC29909.1; -; Genomic_DNA.
DR   RefSeq; XP_003293570.1; XM_003293522.1.
DR   AlphaFoldDB; F1A1M6; -.
DR   STRING; 5786.F1A1M6; -.
DR   EnsemblProtists; EGC29909; EGC29909; DICPUDRAFT_58554.
DR   GeneID; 10504885; -.
DR   KEGG; dpp:DICPUDRAFT_58554; -.
DR   eggNOG; KOG3340; Eukaryota.
DR   InParanoid; F1A1M6; -.
DR   OMA; WESTDKH; -.
DR   OrthoDB; 2955544at2759; -.
DR   Proteomes; UP000001064; Unassembled WGS sequence.
DR   GO; GO:0005764; C:lysosome; IBA:GO_Central.
DR   GO; GO:0004560; F:alpha-L-fucosidase activity; IBA:GO_Central.
DR   GO; GO:0006004; P:fucose metabolic process; IBA:GO_Central.
DR   GO; GO:0016139; P:glycoside catabolic process; IBA:GO_Central.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR   InterPro; IPR016286; FUC_metazoa-typ.
DR   InterPro; IPR031919; Fucosidase_C.
DR   InterPro; IPR000933; Glyco_hydro_29.
DR   InterPro; IPR018526; Glyco_hydro_29_CS.
DR   InterPro; IPR013780; Glyco_hydro_b.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR10030; ALPHA-L-FUCOSIDASE; 1.
DR   PANTHER; PTHR10030:SF46; ALPHA-L-FUCOSIDASE-RELATED; 1.
DR   Pfam; PF01120; Alpha_L_fucos; 1.
DR   Pfam; PF16757; Fucosidase_C; 1.
DR   PIRSF; PIRSF001092; Alpha-L-fucosidase; 1.
DR   PRINTS; PR00741; GLHYDRLASE29.
DR   SMART; SM00812; Alpha_L_fucos; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   PROSITE; PS00385; ALPHA_L_FUCOSIDASE; 1.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|PIRNR:PIRNR001092};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR001092};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001064};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|PIRNR:PIRNR001092}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|PIRNR:PIRNR001092"
FT   CHAIN           22..440
FT                   /note="alpha-L-fucosidase"
FT                   /evidence="ECO:0000256|PIRNR:PIRNR001092"
FT                   /id="PRO_5016196560"
FT   DOMAIN          350..437
FT                   /note="Alpha-L-fucosidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16757"
FT   SITE            268
FT                   /note="May be important for catalysis"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001092-1"
SQ   SEQUENCE   440 AA;  50406 MW;  55E4D3CC23633C2F CRC64;
     MDILKIITIV ILLIFVNIVN SQYSANWTEL NKRPNPAWYD EVKFGIFIHF GIYSVPAFNN
     GSYAEWYWWN LETGNFAPMF NLRDFDANDW AQTIEKSGAK YVVLTSKHHE GYTLWQSNQS
     WNWNSVDNGP GIDIVGELTK AVKNLGMHMG LYHSLYEWYN PLYNSDKDSG NPPKKDVYVQ
     QVLMPMLMDL VNTYEPHIIW ADGEWEQTSS YWKSTEFLSW LYSDSPVKDQ VVVNDRWGSE
     CRGVDGGFFT GNDHWQPGHL VSHKWENCET FDNSYGYNQF QPAKAYSNST ELIREFVETV
     ACGGNFLLDI GPDSEGVIPI NEQNNLLDMG FWLQINGEAI YGSSPWRVQN QTESIWFTTN
     TTNGNVYAFV YEYPETGQIV LKDPQCKSSS VVTLLGFKSS AKITTQLPKN DQPGITLNLP
     FAAPQDYPPF VYVFKFTGCE
//
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